Send to

Choose Destination
Cold Spring Harb Perspect Med. 2016 Jul 1;6(7). pii: a024398. doi: 10.1101/cshperspect.a024398.

The Prion-Like Properties of Amyloid-β Assemblies: Implications for Alzheimer's Disease.

Author information

Yerkes National Primate Research Center and Department of Neurology, Emory University, Atlanta, Georgia 30322.
Department of Cellular Neurology, Hertie Institute for Clinical Brain Research, University of Tübingen, D-72076 Tübingen, Germany German Center for Neurodegenerative Diseases (DZNE), D-72076 Tübingen, Germany.


Since the discovery that prion diseases can be transmitted to experimental animals by inoculation with afflicted brain matter, researchers have speculated that the brains of patients suffering from other neurodegenerative diseases might also harbor causative agents with transmissible properties. Foremost among these disorders is Alzheimer's disease (AD), the most common cause of dementia in the elderly. A growing body of research supports the concept that the pathogenesis of AD is initiated and sustained by the endogenous, seeded misfolding and aggregation of the protein fragment amyloid-β (Aβ). At the molecular level, this mechanism of nucleated protein self-assembly is virtually identical to that of prions consisting of the prion protein (PrP). The formation, propagation, and spread of Aβ seeds within the brain can thus be considered a fundamental feature of AD pathogenesis.

[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for HighWire Icon for PubMed Central
Loading ...
Support Center